Cited by 797TGF-β signaling in diseasesDevelopmental Biology and Gene RegulationSignaling Pathways in Disease

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Specificity, versatility, and control of TGF-β family signaling

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Derynck, Rik, Budi, Erine H.·2019·Science Signaling

DOI 10.1126/scisignal.aav5183PMC PMC6800142

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Abstract

Molecular function and pathway cross-talk in TGF-β signaling reveal its complexity and open questions.

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Transforming Growth Factor β-Induced Smad1/5 Phosphorylation in Epithelial Cells Is Mediated by Novel Receptor Complexes and Is Essential for Anchorage-Independent Growth
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A Smad action turnover switch operated by WW domain readers of a phosphoserine codePreprint
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Specificity of Drosophila Cytonemes for Distinct Signaling Pathways
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BMP2-induced Apoptosis Is Mediated by Activation of the TAK1-p38 Kinase Pathway That Is Negatively Regulated by Smad6
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Bone Morphogenetic Protein-2-Induced Signaling and Osteogenesis Is Regulated by Cell Shape, RhoA/ROCK, and Cytoskeletal Tension
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SIRT1 Inhibits Transforming Growth Factor β-Induced Apoptosis in Glomerular Mesangial Cells via Smad7 Deacetylation
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Transforming Growth Factor-β1 (TGF-β)–induced Apoptosis of Prostate Cancer Cells Involves Smad7-dependent Activation of p38 by TGF-β-activated Kinase 1 and Mitogen-activated Protein Kinase Kinase 3
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Activation of p21ras by transforming growth factor beta in epithelial cells.
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TRAF4 Promotes TGF-β Receptor Signaling and Drives Breast Cancer Metastasis
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Dual Roles of Cripto as a Ligand and Coreceptor in the Nodal Signaling Pathway
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“Cripto enables Nodal binding to the activin receptor complex, thus activating Nodal signaling, whereas its absence promotes activin signaling and prevents Nodal signaling (75, 89, 90).”
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Structural Basis of Heteromeric Smad Protein Assembly in TGF-β Signaling
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Integration of TGF-ß and Ras/MAPK Signaling Through p53 Phosphorylation
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R. Derynck K. Miyazono The Biology of the TGF-β Family (Cold Spring Harbor Laboratory Press 2017) pp. 1164.

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Authors: Derynck, R., & Budi, E. H.
Affiliations: University of California, San Francisco (US)
Corresponding author: Derynck, Rik
ORCID: Derynck, Rik
Budi, Erine H.
Venue: Science Signaling
Publisher: American Association for the Advancement of Science (AAAS)
Published: 2019-02-26
Volume: 12
Issue: 570
ISSN: 1937-9145 (ISSN-L)
1945-0877
DOI: 10.1126/scisignal.aav5183
PMC: PMC6800142
OpenAlex: W2917714624
Cited by: 785
References: 347
Citations by year: 2026: 83 · 2025: 85 · 2024: 129 · 2023: 118 · 2022: 102 · 2021: 152 · 2020: 77 · 2019: 35
FWCI: 8.08
Type: journal article
Language: en
Open access: bronze
doi.org
Locations: Science Signaling (publishedVersion)
PubMed (publishedVersion)
PubMed Central (acceptedVersion)
eScholarship (California Digital Library) (submittedVersion)
Funders: National Cancer Institute (RO1-CA63101, RO1-CA136690)
JDRF (3-APF-2017-392-A-N)
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › TGF-β signaling in diseases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Developmental Biology and Gene Regulation
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
Keywords: Smad proteins, TGF-beta receptor, dual-specificity kinase, signaling crosstalk, non-Smad signaling, cancer, fibrosis, developmental anomalies
MeSH terms: Animals, Cell Differentiation, Gene Expression Regulation, Humans, Ligands, Neoplasms, Protein Binding, Signal Transduction, Transforming Growth Factor beta, Receptors, Transforming Growth Factor beta

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